Structural highlights
Function
NROR_PYRFU Catalyzes the NADH-dependent reduction of rubredoxin (Rd), a small iron-containing redox protein (PubMed:10464233, PubMed:11398485, PubMed:15746356). Can also reduce other electron carriers, including 2,6-dichlorophenol indophenol, benzyl viologen and menadione, but rubredoxin is the most efficient electron acceptor (PubMed:10464233, PubMed:11398485, PubMed:15746356). Does not reduce ferredoxin (PubMed:10464233). Shows comparable activity with NADPH and NADH as electron donors, but NADPH is probably the preferred physiological electron donor (PubMed:10464233, PubMed:11398485). Is probably part of an oxygen detoxification system that protects P.furiosus during exposure to oxygen (PubMed:15746356).[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Ma K, Adams MW. A hyperactive NAD(P)H:Rubredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol. 1999 Sep;181(17):5530-3. PMID:10464233 doi:10.1128/JB.181.17.5530-5533.1999
- ↑ Ma K, Adams MW. NAD(P)H:rubredoxin oxidoreductase from Pyrococcus furiosus. Methods Enzymol. 2001;334:55-62. PMID:11398485 doi:10.1016/s0076-6879(01)34458-0
- ↑ Grunden AM, Jenney FE Jr, Ma K, Ji M, Weinberg MV, Adams MW. In vitro reconstitution of an NADPH-dependent superoxide reduction pathway from Pyrococcus furiosus. Appl Environ Microbiol. 2005 Mar;71(3):1522-30. PMID:15746356 doi:10.1128/AEM.71.3.1522-1530.2005
